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Crystal structure of a glutathione S-transferase SBGSTU7 from salix babylonica

Analyse Crystal structure of a glutathione S-transferase SBGSTU7 from salix babylonica in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7DWD
Type
protein
Length
212 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Glutathione S-transferase
UniProt
A0A4Y5R087
Pockets
3 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 58% helix, 9% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGlutathione S-transferaseprotein21258% helix, 9% strandA0A4Y5R087

Pockets

3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12940.630.7939empty
21000.380.7521empty
3750.330.7519empty

Compared structures

  • 7DWD · Crystal structure of a glutathione S-transferase SbGSTU7 from Salix babylonica · the same entry in another collection · chain A against A, TM-score 1.00

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